Nanocrystalline protein domains via salting-out
Date
2021-11-02
Journal Title
Journal ISSN
Volume Title
Publisher
Acta Crystallographica Section F: Structural Biology Communications
Abstract
Protein salting-out is a well established phenomenon that in many cases leads to amorphous structures and protein gels, which are usually not considered to be useful for protein structure determination. Here, microstructural measurements of several different salted-out protein dense phases are reported, including of lysozyme, ribonuclease A and an IgG1, showing that salted-out protein gels unexpectedly contain highly ordered protein nanostructures that assemble hierarchically to create the gel. The nanocrystalline domains are approximately 10–100 nm in size, are shown to have structures commensurate with those of bulk crystals and grow on time scales in the order of an hour to a day. Beyond revealing the rich, hierarchical nanoscale to mesoscale structure of protein gels, the nanocrystals that these phases contain are candidates for structural biology on next-generation X-ray free-electron lasers, which may enable the study of biological macromolecules that are difficult or impossible to crystallize in bulk.
Description
This article was originally published in Acta Crystallographica Section F: Structural Biology Communications. The version of record is available at: https://doi.org/10.1107/S2053230X21009961
Keywords
protein crystallization, salting-out, X-ray free-electron lasers, small-angle scattering
Citation
Greene, D.G., Modla, S., Sandler, S.I., Wagner, N.J. and Lenhoff, A.M. (2021), Nanocrystalline protein domains via salting-out. Acta Cryst. F, 77: 412-419. https://doi.org/10.1107/S2053230X21009961